PMC:4504005 / 20277-21156 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4504005","sourcedb":"PMC","sourceid":"4504005","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4504005","text":"The positions of RAMP1 and RAMP2 relative to CLR differ in the two structures and the RAMPs elicit subtly different CLR conformations (Figure 6A). Equivalent RAMP1/2 Cα positions at the end of α2 differ by ∼3 to 4.5 Å such that RAMP2 α2 is closer to the peptide-binding site than RAMP1 α2. A similar 3 to 4.5 Å displacement of the RAMP1/2 α3 helices is accompanied by shifts in the position of the C-terminal end of CLR α1 (Figures 6A and 6B). The RAMPs and CLR α1 appear to move somewhat as a unit relative to the remainder of CLR, which is also evident in the comparisons of the peptide-bound structures to the ligand-free and small molecule antagonist-bound structures (Figures 3A, 3E, and 3F). The subtly different CLR loop 2 positions in the structures may reflect RAMP-dependent differences at the interface with CLR α1 propagated to loop 2 via CLR W69 (Figures 6A and 6B).","tracks":[]}